ID A0A0Q5QRM0_9SPHN Unreviewed; 523 AA.
AC A0A0Q5QRM0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=ASG11_14595 {ECO:0000313|EMBL:KQS02029.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS02029.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS02029.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS02029.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS02029.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS02029.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043839};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQS02029.1}.
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DR EMBL; LMPM01000002; KQS02029.1; -; Genomic_DNA.
DR RefSeq; WP_055781664.1; NZ_LMPM01000002.1.
DR AlphaFoldDB; A0A0Q5QRM0; -.
DR STRING; 1736350.ASG11_14595; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000051080; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR Gene3D; 6.20.440.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KQS02029.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000051080}.
FT DOMAIN 185..302
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 383..482
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 55566 MW; D982A601FF16ED37 CRC64;
MSINASGWRP EAPQQGTSAA PTFTGNKALM LEEALIFEIG DTTTTGVEVA APAKVQSRLG
ELARTTAIGL PGLSEPETVR HYTRLSRQNY GIDLGFFPLG SCTMKHNPRL NEKMARLPGF
ADVHPLAPVD TVQGALGVIN ELAVWLIELT GMYGVAMTPK AGAHGELCGI LCIKAALEKR
GEGHRKVVLV PESAHGTNPA TAAFAGFKVE DIPATAEGRV DLDALKSRLG PDVAAVMITN
PNTCGLFERD MKAISDAVHA AGGYVYCDGA NFNAIVGRVR PGDLGIDAMH INLHKTFSTP
HGGGGPGSGP VVLSEALAPF GPLPFTERHA DGHITLVEEE TVDDRHPDSF GRMTAFNGQM
GMFTRALTYI LSHGADGLRQ VAEDAVLNAN YILRSLDKTL VAPFGPSGPC MHEALFSDEN
LAEGFSTIDV AKGLIDEGYH PMTMYFPLVV HGAMLIEPTE TESKAALDQF IGALRSVAER
AKAGDVALKS APHFAPRSRL DETLAARKPV LVWKDPVLAE AAE
//
